Difference between revisions of "AcsA"
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− | <pubmed> 19136592, 18487328, 12850135 </pubmed> | + | <pubmed>12618455, 19136592, 18487328, 12850135 </pubmed> |
# Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] | # Author1, Author2 & Author3 (year) Title ''Journal'' '''volume:''' page-page. [http://www.ncbi.nlm.nih.gov/sites/entrez/PMID PubMed] |
Revision as of 11:44, 12 June 2009
- Description: acetyl-CoA synthetase
Gene name | acsA |
Synonyms | |
Essential | no |
Product | acetyl-CoA synthetase) |
Function | utilization of acetate, fatty acids |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 64 kDa, 5.547 |
Gene length, protein length | 1716 bp, 572 aa |
Immediate neighbours | tyrS, acuA |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU29680
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA (according to Swiss-Prot)
- Protein family: ATP-dependent AMP-binding enzyme family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification: acetylated on Lys-549 by AcuA, this results in inactivation PubMed, deacetylated by SrtN and AcuC deacetylates (and thereby activates) AcsA PubMed
- Cofactor(s):
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure:
- Swiss prot entry: P39062
- KEGG entry: [3]
- E.C. number: 6.2.1.1
Additional information
Expression and regulation
- Operon: acsA
- Regulatory mechanism: CodY: transcription repression PubMed1 PubMed2, CcpA: transcription repression
- Additional information:
Biological materials
- Mutant:
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
Your additional remarks
References
Jeffrey G Gardner, Jorge C Escalante-Semerena
In Bacillus subtilis, the sirtuin protein deacetylase, encoded by the srtN gene (formerly yhdZ), and functions encoded by the acuABC genes control the activity of acetyl coenzyme A synthetase.
J Bacteriol: 2009, 191(6);1749-55
[PubMed:19136592]
[WorldCat.org]
[DOI]
(I p)
Jeffrey G Gardner, Jorge C Escalante-Semerena
Biochemical and mutational analyses of AcuA, the acetyltransferase enzyme that controls the activity of the acetyl coenzyme a synthetase (AcsA) in Bacillus subtilis.
J Bacteriol: 2008, 190(14);5132-6
[PubMed:18487328]
[WorldCat.org]
[DOI]
(I p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
Virginie Molle, Yoshiko Nakaura, Robert P Shivers, Hirotake Yamaguchi, Richard Losick, Yasutaro Fujita, Abraham L Sonenshein
Additional targets of the Bacillus subtilis global regulator CodY identified by chromatin immunoprecipitation and genome-wide transcript analysis.
J Bacteriol: 2003, 185(6);1911-22
[PubMed:12618455]
[WorldCat.org]
[DOI]
(P p)
- Author1, Author2 & Author3 (year) Title Journal volume: page-page. PubMed